ID E2PSR7_ASPNC Unreviewed; 559 AA.
AC E2PSR7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=An07g06000 {ECO:0000313|EMBL:CAK48970.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK48970.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK48970.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000225};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312}.
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DR EMBL; AM270133; CAK48970.1; -; Genomic_DNA.
DR RefSeq; XP_001391678.1; XM_001391641.2.
DR AlphaFoldDB; E2PSR7; -.
DR EnsemblFungi; CAK48970; CAK48970; An07g06000.
DR GeneID; 4981867; -.
DR KEGG; ang:An07g06000; -.
DR VEuPathDB; FungiDB:An07g06000; -.
DR HOGENOM; CLU_004553_2_1_1; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000006706; Chromosome 4L.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:EnsemblFungi.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:EnsemblFungi.
DR CDD; cd04320; AspRS_cyto_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:CAK48970.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 247..559
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 62035 MW; EB80B3820061495B CRC64;
MADSELPTRP KPEETPAAAA APAEGAETSK SASKNAAKKA AKEKAKAEKA AARAAQEKAQ
AAAAAADDTA KDLYGKLPES EDVIAATRFS DISDEHYEKE VTLVARVDNA RVQSAKLAFL
MLRQQGQKLQ AVIALAEPIS RQMIKYTGGL NVNSIVQVTG IIKKPAVPIS SATLSNHEIH
IRKVYMISEA AQMLPMQVKD AERPPPETSE EGFEVGEDGA PIVTLKTRLD NRVLDLQTET
SQAITWISSG VAELFAEYMI KSGSRWIFTP KLVGAATEGG SNVFEVKYFK KNAYLAQSPQ
LYKQMCIAGD MESVFEIAPV FRAEDSNTHR HLTEFAGLDF EKTFRGHYHE VLEFAENLLV
FILSQLKERY ADKIAIIQKS YPKAGDFKLP KDGKALRLNY MDGVAMLKEA GVDVSEQERF
ENDFTTAMEK QLGQIIRDKY DTDFYVLDKF PMAVRPFYTK ACPQDPRFSN SYDFFMRGEE
IMSGAQRIND IKELEESMVA KGLNPNQEGF EDYLSAFRQG CPPHAGGGLG LNRIVMFFLG
LPNVRLASLF PRDPQRLRP
//
